Comparisons of recombinant resilin-like proteins: Repetitive domains are sufficient to confer resilin-like properties

Lyons, RE, Nairn, KM, Huson, MG, Kim, M, Dumsday, G and Elvin, CM (2009) Comparisons of recombinant resilin-like proteins: Repetitive domains are sufficient to confer resilin-like properties. Biomacromolecules, 10 11: 3009-3014. doi:10.1021/bm900601h


Author Lyons, RE
Nairn, KM
Huson, MG
Kim, M
Dumsday, G
Elvin, CM
Title Comparisons of recombinant resilin-like proteins: Repetitive domains are sufficient to confer resilin-like properties
Journal name Biomacromolecules   Check publisher's open access policy
ISSN 1525-7797
1526-4602
Publication date 2009-11-09
Sub-type Article (original research)
DOI 10.1021/bm900601h
Volume 10
Issue 11
Start page 3009
End page 3014
Total pages 6
Place of publication Washington, DC, U.S.A.
Publisher American Chemical Society
Language eng
Formatted abstract
Two novel recombinant proteins An16 and Dros16 have recently been generated. These recombinant proteins contain, respectively, sixteen copies of an 11 amino acid repetitive domain (AQTPSSQYGAP) observed in a resilin-like gene from Anopheles gambiae and sixteen copies of a 15 amino acid repetitive domain (GGRPSDSYGAPGGGN) observed in the first exon of the Drosophila melanogaster CG15920 gene. We compare structural characteristics of the proteins and material properties of resulting biopolymers relative to Rec1-resilin, a previously characterized resilin-like protein encoded by the first exon of the Drosophila melanogaster CG15920 gene. While the repetitive domains of natural resilins display significant variation both in terms of amino acid sequence and length, our synthetic polypeptides have been designed as perfect repeats. Using techniques including circular dichroism, atomic force microscopy, and tensile testing, we demonstrate that both An16 and Dros16 have similar material properties to those previously observed in insect and recombinant resilins. Modulus, elasticity, resilience, and dityrosine content in the cross-linked biomaterials were assessed. Despite the reduced complexity of the An16 and Dros16 proteins compared to natural resilins, we have been able to produce elastic and resilient biomaterials with similar properties to resilin.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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Created: Mon, 11 Apr 2011, 10:36:17 EST by Ms Misook Kim on behalf of School of Chemistry & Molecular Biosciences